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5MP1_MOUSE
ID   5MP1_MOUSE              Reviewed;         419 AA.
AC   Q91VK1; Q9D0N4;
DT   31-OCT-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   03-AUG-2022, entry version 131.
DE   RecName: Full=eIF5-mimic protein 1 {ECO:0000250|UniProtKB:Q9Y6E2};
DE   AltName: Full=Basic leucine zipper and W2 domain-containing protein 2;
GN   Name=Bzw2; Synonyms=5mp1 {ECO:0000250|UniProtKB:Q9Y6E2};
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J; TISSUE=Embryo;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N; TISSUE=Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic brain;
RX   PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA   Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT   "Phosphoproteomic analysis of the developing mouse brain.";
RL   Mol. Cell. Proteomics 3:1093-1101(2004).
RN   [4]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-412, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Brown adipose tissue, Heart, Kidney, Lung, Pancreas, and Spleen;
RX   PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA   Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA   Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT   "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL   Cell 143:1174-1189(2010).
CC   -!- FUNCTION: Translation initiation regulator which represses non-AUG
CC       initiated translation and repeat-associated non-AUG (RAN) initiated
CC       translation by acting as a competitive inhibitor of eukaryotic
CC       translation initiation factor 5 (EIF5) function (By similarity).
CC       Increases the accuracy of translation initiation by impeding EIF5-
CC       dependent translation from non-AUG codons by competing with it for
CC       interaction with EIF2S2 within the 43S pre-initiation complex (PIC) in
CC       an EIF3C-binding dependent manner (By similarity).
CC       {ECO:0000250|UniProtKB:Q9Y6E2}.
CC   -!- SUBUNIT: Interacts with EIF3E, EIF2S2 and EIF3C.
CC       {ECO:0000250|UniProtKB:Q9Y6E2}.
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:Q9Y6E2}.
CC   -!- SIMILARITY: Belongs to the BZW family. {ECO:0000305}.
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DR   EMBL; AK011253; BAB27495.1; -; mRNA.
DR   EMBL; AK160544; BAE35861.1; -; mRNA.
DR   EMBL; BC013060; AAH13060.1; -; mRNA.
DR   CCDS; CCDS25884.1; -.
DR   RefSeq; NP_080116.2; NM_025840.3.
DR   AlphaFoldDB; Q91VK1; -.
DR   SMR; Q91VK1; -.
DR   BioGRID; 211804; 7.
DR   IntAct; Q91VK1; 4.
DR   MINT; Q91VK1; -.
DR   STRING; 10090.ENSMUSP00000020856; -.
DR   iPTMnet; Q91VK1; -.
DR   PhosphoSitePlus; Q91VK1; -.
DR   EPD; Q91VK1; -.
DR   jPOST; Q91VK1; -.
DR   MaxQB; Q91VK1; -.
DR   PaxDb; Q91VK1; -.
DR   PeptideAtlas; Q91VK1; -.
DR   PRIDE; Q91VK1; -.
DR   ProteomicsDB; 273781; -.
DR   Antibodypedia; 11817; 105 antibodies from 25 providers.
DR   DNASU; 66912; -.
DR   Ensembl; ENSMUST00000020856; ENSMUSP00000020856; ENSMUSG00000020547.
DR   GeneID; 66912; -.
DR   KEGG; mmu:66912; -.
DR   UCSC; uc007njp.2; mouse.
DR   CTD; 28969; -.
DR   MGI; MGI:1914162; Bzw2.
DR   VEuPathDB; HostDB:ENSMUSG00000020547; -.
DR   eggNOG; KOG2297; Eukaryota.
DR   GeneTree; ENSGT00390000012561; -.
DR   HOGENOM; CLU_032849_0_1_1; -.
DR   InParanoid; Q91VK1; -.
DR   OMA; ELIQCIW; -.
DR   OrthoDB; 653740at2759; -.
DR   PhylomeDB; Q91VK1; -.
DR   TreeFam; TF324313; -.
DR   BioGRID-ORCS; 66912; 5 hits in 73 CRISPR screens.
DR   ChiTaRS; Bzw2; mouse.
DR   PRO; PR:Q91VK1; -.
DR   Proteomes; UP000000589; Chromosome 12.
DR   RNAct; Q91VK1; protein.
DR   Bgee; ENSMUSG00000020547; Expressed in cortical plate and 264 other tissues.
DR   ExpressionAtlas; Q91VK1; baseline and differential.
DR   Genevisible; Q91VK1; MM.
DR   GO; GO:0005737; C:cytoplasm; ISS:UniProtKB.
DR   GO; GO:0006446; P:regulation of translational initiation; ISS:UniProtKB.
DR   CDD; cd11560; W2_eIF5C_like; 1.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR043510; W2_BZW1/2.
DR   InterPro; IPR003307; W2_domain.
DR   Pfam; PF02020; W2; 1.
DR   SMART; SM00515; eIF5C; 1.
DR   SUPFAM; SSF48371; SSF48371; 1.
DR   PROSITE; PS51363; W2; 1.
PE   1: Evidence at protein level;
KW   Acetylation; Cytoplasm; Phosphoprotein; Reference proteome;
KW   Translation regulation.
FT   CHAIN           1..419
FT                   /note="eIF5-mimic protein 1"
FT                   /id="PRO_0000254620"
FT   DOMAIN          248..415
FT                   /note="W2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00695"
FT   REGION          1..22
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         117
FT                   /note="N6-acetyllysine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6E2"
FT   MOD_RES         412
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21183079"
FT   MOD_RES         414
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9Y6E2"
FT   MOD_RES         419
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9WTT7"
FT   CONFLICT        69
FT                   /note="F -> L (in Ref. 1; BAB27495)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        326
FT                   /note="A -> R (in Ref. 1; BAB27495)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   419 AA;  48063 MW;  996FC462B50EAF6F CRC64;
     MNKHQKPVLT GQRFKTRKRD EKEKFEPTVF RDTLVQGLNE AGDDLEAVAK FLDSTGSRLD
     YRRYADTLFD ILVAGSMLAP GGTRIDDGDK TKMTNHCVFS ANEDHETIRN YAQVFNKLIR
     RYKYLEKAFE DEMKKLLLFL KAFSEAEQTK LAMLSGILLG NGTLPATILT SLFTDSLVKE
     GIAASFAVKL FKAWMAEKDA NSVTSSLRKA NLDKRLLELF PVNRQSVDHF AKYFTDAGLK
     ELSDFLRVQQ SLGTRKELQK ELQERLSQEC PIKEVVLYVK EEMKRNDLPE TAVIGLLWTC
     IMNAVEWNKK EELVAEQALK HLKQYAPLLA VFSSQGQSEL VLLQKVQEYC YDNIHFMKAF
     QKIVVLFYKA DVLSEEAILK WYKEAHAAKG KSVFLDQMKK FVEWLQNAEE ESESEGEES
 
 
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